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Citation and License

Nanoscale Research Letters 2013, 8:180
doi:10.1186/1556-276X-8-180

Published: 19 April 2013

Abstract

Lipases are one of the most important biocatalysts for biotechnological applications.
Immobilization is an efficient method to increase the stability and reusability of
lipases. In this study, nanoporous gold (NPG), a new kind of nanoporous material with
tunable porosity and excellent biocompatibility, was employed as an effective support
for lipase immobilization. The pore size of NPG and adsorption time played key roles
in the construction of lipase-NPG biocomposites. The morphology and composition of
NPG before and after lipase loading are verified using a scanning electron microscope,
equipped with an energy-dispersive X-ray spectrometer. The resulting lipase-NPG biocomposites
exhibited excellent catalytic activity and remarkable reusability. The catalytic activity
of the lipase-NPG biocomposite with a pore size of 35 nm had no decrease after ten
recycles. Besides, the lipase-NPG biocomposite exhibited high catalytic activity in
a broader pH range and higher temperature than that of free lipase. In addition, the
leaching of lipase from NPG could be prevented by matching the protein’s diameter
and pore size. Thus, the encapsulation of enzymes within NPG is quite useful for establishing
new functions and will have wide applications for different chemical processes.